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@ARTICLE{Fejzagi:884300,
      author       = {Fejzagić, Alexander V. and Myllek, Sebastian and
                      Hogenkamp, Fabian and Greb, Julian and Pietruszka, Jörg and
                      Classen, Thomas},
      title        = {{A} {F}luorescence‐{B}ased {A}ssay {S}ystem for the
                      {D}etermination of {H}aloperoxidase‐{A}ctivity {U}sing a
                      {T}wo‐{D}imensional {C}alibration {A}p‐proach},
      journal      = {ChemistryOpen},
      volume       = {9},
      number       = {9},
      issn         = {2191-1363},
      address      = {Weinheim},
      publisher    = {Wiley-VCH-Verl.},
      reportid     = {FZJ-2020-03186},
      pages        = {959 - 966},
      year         = {2020},
      abstract     = {Screening for an interesting biocatalyst and its subsequent
                      kinetic characterization depends on a reliable activity
                      assay. In this work, a fluorometric assay based on the
                      halogenation of 4‐methyl‐7‐diethylamino‐coumarin was
                      established to monitor haloperoxidase‐activity. Since
                      haloperoxidases utilize hydrogen peroxide and halide ions to
                      halogenate a broad range of substrates by releasing
                      hypohalous acids, a direct quantification of
                      haloperoxidase‐activity remains difficult. With the system
                      presented here,
                      3‐bromo‐4‐methyl‐7‐diethylaminocoumarin is
                      preferentially formed and monitored by fluorescence
                      measurements. As starting material and product share similar
                      spectroscopical properties, a two‐dimensional calibration
                      ap‐proach was utilized to allow for quantification of each
                      compound within a single measurement. To validate the
                      system, the two‐dimensional Michaelis‐Menten kinetics of
                      a vanadium‐dependent chloroperoxidase from Curvularia
                      inaequalis were recorded, yielding the first overall kinetic
                      parameters for this enzyme. With limits of detection and
                      quantification in the low μm range, this assay may provide
                      a reliable alternative system for the quantification of
                      haloperoxidase‐activity.},
      cin          = {IBG-1 / IBOC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-1-20101118 / I:(DE-Juel1)IBOC-20090406},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32995110},
      UT           = {WOS:000573591700008},
      doi          = {10.1002/open.202000184},
      url          = {https://juser.fz-juelich.de/record/884300},
}